Formation in vivo, purification and crystallization of a complex of the gamma and epsilon subunits of the F0F1-ATPase of Escherichia coli.
J Mol Biol
; 229(4): 1159-62, 1993 Feb 20.
Article
em En
| MEDLINE
| ID: mdl-8445643
ABSTRACT
A complex comprising the epsilon subunit of Escherichia coli F1-ATPase (ECF1-ATPase) and a glutathione-S-transferase gamma subunit (of ECF1-ATPase) fusion protein was formed in vivo and purified from cell extracts by binding to glutathione-agarose beads. The glutathione-S-transferase was released from the complex by digestion with thrombin and the gamma/epsilon complex purified by cation-exchange chromatography. Crystals of the complex were grown by vapour diffusion using PEG8000 as precipitant. The crystals are orthorhombic, space-group P2(1)2(1)2 with a = 161.9 A, b = 44.1 A and c = 63.4 A. The volume of the asymmetric unit is consistent with the presence of a complex of one gamma subunit and one epsilon subunit.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
ATPases Translocadoras de Prótons
/
Escherichia coli
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
1993
Tipo de documento:
Article